| http://purl.uniprot.org/citations/11399750 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11399750 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11399750 | http://www.w3.org/2000/01/rdf-schema#comment | "Vacuolar H(+)-ATPases (V-ATPases) are essential for acidification of intracellular compartments and for proton secretion from the plasma membrane in kidney epithelial cells and osteoclasts. The cellular proteins that regulate V-ATPases remain largely unknown. A screen for proteins that bind the V-ATPase E subunit using the yeast two-hybrid assay identified the cDNA clone coded for aldolase, an enzyme of the glycolytic pathway. The interaction between E subunit and aldolase was confirmed in vitro by precipitation assays using E subunit-glutathione S-transferase chimeric fusion proteins and metabolically labeled aldolase. Aldolase was isolated associated with intact V-ATPase from bovine kidney microsomes and osteoclast-containing mouse marrow cultures in co-immunoprecipitation studies performed using an anti-E subunit monoclonal antibody. The interaction was not affected by incubation with aldolase substrates or products. In immunocytochemical assays, aldolase was found to colocalize with V-ATPase in the renal proximal tubule. In osteoclasts, the aldolase-V-ATPase complex appeared to undergo a subcellular redistribution from perinuclear compartments to the ruffled membranes following activation of resorption. In yeast cells deficient in aldolase, the peripheral V(1) domain of V-ATPase was found to dissociate from the integral membrane V(0) domain, indicating direct coupling of glycolysis to the proton pump. The direct binding interaction between V-ATPase and aldolase may be a new mechanism for the regulation of the V-ATPase and may underlie the proximal tubule acidification defect in hereditary fructose intolerance."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m008768200"xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m008768200"xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Lu M."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Lu M."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Zhang L."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Zhang L."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Dunn W.A. Jr."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Dunn W.A. Jr."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Gluck S.L."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Gluck S.L."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Holliday L.S."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/author | "Holliday L.S."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/pages | "30407-30413"xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/pages | "30407-30413"xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/title | "Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/title | "Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump."xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/volume | "276"xsd:string |
| http://purl.uniprot.org/citations/11399750 | http://purl.uniprot.org/core/volume | "276"xsd:string |